The vitamin D receptor (VDR) is a protein that is turned on by calciferol. It is interested in maintaining the mineral harmony in the body and adding to growth and hair production. It also interacts with adipose cells.

VDRs happen to be expressed inside the parathyroid glands, intestines, epithelial virtual data room comparison skin cells, and many defense cell types. They are believed to regulate the intestinal absorption of calcium supplements, and to mediate some of the associated with vitamin D on bone maintenance. Fortunately they are thought to perform an important position in metabolism.

VDR can be found in a variety of tissue, including epithelial cells, macrophages, neutrophils, and skin keratinocytes. However , they can be most widely expressed in the kidneys and bones.

The VDR is phosphorylated about serine residues by many protein kinases. These kinases include PKA and PKC. The effect of such kinases upon VDR is normally ligand structured. Specifically, the phosphorylation of Ser51 simply by PKC decreased VDR nuclear localization. Likewise, phosphorylation of Ser182 by PKA reduced RXR heterodimerization.

Studies have shown that VDRs exist in a part of glial cells, particularly in oligodendrocytes in white matter. Although VDR immunoreactivity has been found in a number of glial cell lines, no data has been shown that the occurrence of VDR in glia is a cause for increased risk of tumorigenesis.

In addition , VDR seems present in a subset of neurons. In fact , nuclear discoloration has been confirmed in real human cortex and glial cell-lines.

A large 220-kDa protein is found in human major glioblastoma cells. In contrast, a small recombinant VDR-like protein was produced.